ArticlePlant physiology2004
Cloning and characterization of two NAD kinases from Arabidopsis. identification of a calmodulin binding isoform.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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55 citing papers in PubMed, 116 citations in OpenAlex.
- A rice calmodulin-like protein OsCML27 participates in drought tolerance by fine-tuning OsRbohB-mediated ROS signaling.Science advances · 2026Article
- Identification of CCR4C as a chloroplast-localized NADP(H) phosphatase regulating NAD(P)(H) balance inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Metabolic changes associated with dark-induced leaf senescence in ArabidopsisPlant signaling & behavior · 2023Article
- Comparative transcriptome analysis of grafting to improve chilling tolerance of cucumber.Protoplasma · 2023Article
- Molecular Regulation and Evolution of Redox Homeostasis in Photosynthetic Machinery.Antioxidants (Basel, Switzerland) · 2022Review
- NADP+ supply adjusts the synthesis of photosystem I in Arabidopsis chloroplasts.Plant physiology · 2022Article
- NAD kinase promoteseLife · 2022Article
- Arabidopsis nitrate-induced aspartate oxidase gene expression is necessary to maintain metabolic balance under nitrogen nutrient fluctuation.Communications biology · 2022Article
- Altered metabolism of chloroplastic NAD kinase-overexpressing Arabidopsis in response to magnesium sulfate supplementation.Plant signaling & behavior · 2021Article
- Indirect Export of Reducing Equivalents From the Chloroplast to Resupply NADP for CFrontiers in plant science · 2021Review
- Polyphosphate-dependent nicotinamide adenine dinucleotide (NAD) kinase: A novel missing link in human mitochondria.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2021Article
- The NAD kinase OsNADK1 affects the intracellular redox balance and enhances the tolerance of rice to drought.BMC plant biology · 2020Article
- Measurement of Chloroplastic NAD Kinase Activity and Whole Tissue NAD Kinase Assay.Bio-protocol · 2020Article
- Identification of the Arabidopsis Calmodulin-Dependent NADPlant physiology · 2019Article
- Limitations of Deuterium-Labelled Substrates for Quantifying NADPH Metabolism in HeterotrophicMetabolites · 2019Article
- Plant peroxisomal solute transporter proteins.Journal of integrative plant biology · 2019Review
- Regulation of Pyridine Nucleotide Metabolism During Tomato Fruit Development Through Transcript and Protein Profiling.Frontiers in plant science · 2019Article
- Inter-Organelle NAD Metabolism Underpinning Light Responsive NADP Dynamics in Plants.Frontiers in plant science · 2019Review
- Physiological Significance of NAD Kinases in Cyanobacteria.Frontiers in plant science · 2019Review
- Calmodulin Is the Fundamental Regulator of NADK-Mediated NAD Signaling in Plants.Frontiers in plant science · 2019Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NAD kinase (NADK; ATP:NAD 2'-phosphotransferase, EC 2.7.1.23), an enzyme found in both prokaryotes and eukaryotes, generates the important pyridine nucleotide NADP from substrates ATP and NAD. The role of NADKs in plants is poorly understood, and cDNAs encoding plant NADKs have not previously been described to our knowledge. We have cloned two cDNAs from Arabidopsis predicted to encode NADK isoforms, designated NADK1 and NADK2, respectively. Expressed as recombinant proteins in bacteria, both NADK1 and NADK2 were catalytically active, thereby confirming their identity as NADKs. Transcripts for both isoforms were detected in all tissues examined and throughout development. Although the predicted catalytic regions for NADK1 and NADK2 show sequence similarity to NADKs from other organisms, NADK2 possesses a large N-terminal extension that appears to be unique to plants. Using recombinant glutathione-S-transferase fusion proteins and calmodulin (CaM)-affinity chromatography, we delineated a Ca2+-dependent CaM-binding domain to a 45-residue region within the N-terminal extension of NADK2. Although recombinant NADK2 was not responsive to CaM in vitro, immunoblot analysis suggests that native NADK2 is a CaM-binding protein. In Arabidopsis crude extracts, CaM-dependent NADK activity was much greater than CaM-independent activity throughout development, particularly in young seedlings. A native CaM-dependent NADK was partially purified from Arabidopsis seedlings (Km NAD=0.20 mM, Km Mg2+ -ATP=0.17 mM). The enzyme was fully activated by conserved CaM (S0.5 = 2.2 nm) in the presence of calcium but displayed differential responsiveness to eight CaM-like Arabidopsis proteins. Possible roles for NADKs in plants are discussed in light of our observations.
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